This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The herpes simplex type-1 virus capsid has a diameter of 1250 [unreadable] and is made up of 4 distinct structural proteins (VP5, VP23, Vp19C and VP26) and a portal complex with a total mass of ~192 MDa. We completed its structure at 8.5 [unreadable] resolution. This represents the largest virus particle solved structurally to such a high resolution. Since then, we have developed a comprehensive approach to study this viral capsid in more detail by a combination of structural prediction, crystallography, single particle reconstruction and electron cryo-tomography.